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Database: UniProt
Entry: A0A6A3B838_HIBSY
LinkDB: A0A6A3B838_HIBSY
Original site: A0A6A3B838_HIBSY 
ID   A0A6A3B838_HIBSY        Unreviewed;      1455 AA.
AC   A0A6A3B838;
DT   17-JUN-2020, integrated into UniProtKB/TrEMBL.
DT   17-JUN-2020, sequence version 1.
DT   02-APR-2025, entry version 14.
DE   SubName: Full=Pectin lyase-like superfamily protein isoform 1 {ECO:0000313|EMBL:KAE8711987.1};
GN   ORFNames=F3Y22_tig00110266pilonHSYRG00067
GN   {ECO:0000313|EMBL:KAE8711987.1};
OS   Hibiscus syriacus (Rose of Sharon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Malvales; Malvaceae; Malvoideae; Hibiscus.
OX   NCBI_TaxID=106335 {ECO:0000313|EMBL:KAE8711987.1, ECO:0000313|Proteomes:UP000436088};
RN   [1] {ECO:0000313|EMBL:KAE8711987.1, ECO:0000313|Proteomes:UP000436088}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Baekdansim {ECO:0000313|Proteomes:UP000436088};
RC   TISSUE=Leaf {ECO:0000313|EMBL:KAE8711987.1};
RA   Kim Y.-M.;
RT   "Draft genome information of white flower Hibiscus syriacus.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the SPT5 family.
CC       {ECO:0000256|ARBA:ARBA00006956}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAE8711987.1}.
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DR   EMBL; VEPZ02000903; KAE8711987.1; -; Genomic_DNA.
DR   Proteomes; UP000436088; Unassembled WGS sequence.
DR   GO; GO:0032044; C:DSIF complex; IEA:TreeGrafter.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003729; F:mRNA binding; IEA:TreeGrafter.
DR   GO; GO:0032784; P:regulation of DNA-templated transcription elongation; IEA:InterPro.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IEA:InterPro.
DR   GO; GO:0006368; P:transcription elongation by RNA polymerase II; IEA:TreeGrafter.
DR   CDD; cd06081; KOW_Spt5_1; 1.
DR   CDD; cd06084; KOW_Spt5_4; 1.
DR   CDD; cd09888; NGN_Euk; 1.
DR   FunFam; 2.30.30.30:FF:000053; Protein RNA-directed DNA methylation 3; 1.
DR   FunFam; 3.30.70.940:FF:000016; Uncharacterized protein; 1.
DR   Gene3D; 2.30.30.30; -; 2.
DR   Gene3D; 3.30.70.940; NusG, N-terminal domain; 1.
DR   InterPro; IPR005824; KOW.
DR   InterPro; IPR041973; KOW_Spt5_1.
DR   InterPro; IPR041977; KOW_Spt5_4.
DR   InterPro; IPR005100; NGN-domain.
DR   InterPro; IPR036735; NGN_dom_sf.
DR   InterPro; IPR039385; NGN_Euk.
DR   InterPro; IPR014722; Rib_uL2_dom2.
DR   InterPro; IPR039659; SPT5.
DR   InterPro; IPR008991; Translation_prot_SH3-like_sf.
DR   PANTHER; PTHR11125:SF8; PROTEIN RNA-DIRECTED DNA METHYLATION 3; 1.
DR   PANTHER; PTHR11125; SUPPRESSOR OF TY 5; 1.
DR   Pfam; PF23042; KOW1_SPT5; 1.
DR   Pfam; PF23291; KOW4_SPT5; 1.
DR   Pfam; PF03439; Spt5-NGN; 1.
DR   SMART; SM00739; KOW; 3.
DR   SUPFAM; SSF50104; Translation proteins SH3-like domain; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000313|EMBL:KAE8711987.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW   Reference proteome {ECO:0000313|Proteomes:UP000436088};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        66..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          289..316
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          509..536
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   DOMAIN          618..645
FT                   /note="KOW"
FT                   /evidence="ECO:0000259|SMART:SM00739"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          566..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          669..692
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          732..1455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..12
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        587..598
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        756..792
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        844..863
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        871..884
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..926
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        944..963
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        976..994
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1010..1021
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1022..1043
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1055..1069
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1088..1103
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1104..1116
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1180..1199
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1215..1226
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1227..1238
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1253..1265
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1322..1332
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1336..1381
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1392..1401
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1435..1445
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1446..1455
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1455 AA;  156193 MW;  05821EF2B818CBDF CRC64;
     MSSKGKEKEV VYGKRKVSAG RSGGVTEESR RKRRNRGVLQ FFEDSAEDDG SDASDGSDIN
     DCKADLINVF FVLFGVFYVS FWSVALYDCL FLRLLGFTPF DFVLHFGFKG FRLWRCLTFS
     RQNDVLQEEP DLDVNKNPWK AHNVPFVPKE EVIEEEFDKM MEERYRGGAR FTTFEEDYEA
     KGSIDKNSTV PPAKDPVIWK VKCVVGRERH SAFCLMQKFI DMKSLGTKLQ IISAFSVDHV
     KGFFFIEADK QCDINEACKG LTYIYSSRLA PVPSNEVYHL LNVRTKCCEI SKGMWARIKN
     GKYKGDLAQV VAVNNEKKKA TVKLIPRIDL QAMAAKFGSG VSISRTVIPA PKLISLIELE
     EFRPLIQFRR DRDTSIGFQV LDGMMLKDGY LYKKVSIDSL SCWGIMPTEE ELLKFSNSDN
     NESDDLEWLS QLYAVTTYQQ LVNNLFHVLF HLHCSRKDFG LIVGMEKDDR YKILREAPEG
     PIVVTVEKHE LKNGPLDTKF TALDKHSKTI SINDTVKVLE GQYEGKQGTV KQIYRGTIFL
     YDENETDNGG FFCCKSPMCE KIKQRSDKCS EKGGDPGGTS DYGDFVSSPK SPISPEKPWQ
     SQEKETKSDF NRGNIDGMFS IGQTLRIRVG PLKGYLCRVL AVYRSDVTVK VGSKQKVLKV
     KNEHLAEVQG KSTAANTNEH DGSTSFKPFG SEASTGDWLN GAGTSAEGGG WNAERCSLSL
     YVLDGEGSAW DTKPTANQNS SWGAAAPSGD NDNKTDGASS AWENNTSTQQ NSAWATGGSD
     HNSNRGSWNN SAPKIDSGGG ASDAWVKTIT GGGPSGASQD VDNDGWDKGK GVAEEGSWGK
     NKKSSVNEGN WNNNDVGSNQ QGSWGIKNDA SVGQDNSWGN TAEKWNNKDG IGGSKGNWGS
     SKPSAEDAKG SWGKQDGGSS LNQSDGWNKE KAADVGTSGG KQDGGSSWYK QLGGSSWGVS
     NTKSGGGAIQ DAGQDSGWSK RSSWNSGSGG TNQEPGWAKK NDSDFGSGDA TKDSTWGKKS
     DWNSGSADAN QESKKNSWGS GTTDAGPDSG WGQRGSWNSG SGNANQNPGW TKKSDSGFAA
     GDATNDSSWE KKGAADASRD SNWGKKSSWG TGTDSGQDAG WGKKGGWNPG SSSAGEDSGW
     KSKSKWNSGA GDANQDSGWK PKNDWKSGSG NEDQNEPFSG RGGGSWRGGF GGRDGSGRGF
     RGRGDSDGGG FRGRGRSDRG RGRSDRGGFG GDGGGYGGRG DRGGDRGGYG GRGGDRGGYR
     GRGGDRGGYG GRGRGRRDEN GGWNNGGDSG ENKSYGWNKE GNQGWNGGGA KTCGQSNADN
     RGQSSGWSQP GGWNKGTGST NEAGGNQDTS WKSSNSSDGN KWSGWNQSTC SKDVKESTSQ
     GHGWEKSSAT AAGGGWGGRG SGSAEQVEPK TADEGASSGW NKPKDGEGSS GNQDAWGKAS
     SSSWGQGSGS RKGGW
//
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